Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH.

@article{Suno2012ConformationalTO,
  title={Conformational transition of the lid helix covering the protease active site is essential for the ATP-dependent protease activity of FtsH.},
  author={Ryoji Suno and Masakazu Shimoyama and Akiko Abe and Tatsuro Shimamura and Natsuka Shimodate and Yo-hei Watanabe and Yoshinori Akiyama and Masasuke Yoshida},
  journal={FEBS letters},
  year={2012},
  volume={586 19},
  pages={3117-21}
}
When bound to ADP, ATP-dependent protease FtsH subunits adopt either an "open" or "closed" conformation. In the open state, the protease catalytic site is located in a narrow space covered by a lidlike helix. This space disappears in the closed form because the lid helix bends at Gly448. Here, we replaced Gly448 with various residues that stabilize helices. Most mutants retained low ATPase activity and bound to the substrate protein, but lost protease activity. However, a mutant proline… CONTINUE READING

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